Molecular characterization of lysyl oxidase‐mediated extracellular matrix remodeling during mouse decidualization

• Published in: FEBS letters Vol. 591; no. 10; pp. 1394 - 1407
• Main Authors: Li, Shu‐Yun, Yan, Jia‐qi, Song, Zhuo, Liu, Yue‐Fang, Song, Min‐Jie, Qin, Jia‐Wen, Yang, Zeng‐Ming, Liang, Xiao‐Huan
• Format: Journal Article
• Language: English
• Published: England 01.05.2017
• Subjects: Animals; beta Catenin - metabolism; Blastocyst - metabolism; Cell Movement; Decidua - physiology; decidualization; Embryo Implantation; Estrogens - metabolism; Extracellular Matrix - metabolism; Extracellular Matrix Proteins - genetics; Extracellular Matrix Proteins - metabolism; Female; Gene Expression Regulation, Developmental; Lox; Mice; Pregnancy; Prolactin - analogs & derivatives; Prolactin - metabolism; Protein-Lysine 6-Oxidase - genetics; Protein-Lysine 6-Oxidase - metabolism; Proto-Oncogene Proteins c-myc - metabolism; Stromal Cells - cytology; uterus; Wnt Signaling Pathway; Lox; decidualization; uterus
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1002/1873-3468.12645

The establishment of decidualization is a prerequisite of successful pregnancy. Lysyl oxidase (Lox) is a copper‐containing amine oxidase which catalyzes cross‐linking of collagen and elastin in the ECM. Lox is expressed in the subluminal stroma surrounding the implanting blastocyst on day 5 of pregnancy. From days 6 to 8, the signals for Lox mRNA and protein are strongly detected in the decidual cells. The expression of Lox is under the control of estrogen via the GSK‐3β/β‐catenin/c‐myc pathway. Dtprp is decreased by the inhibition of Lox activity. Furthermore, the inhibition of Lox activity decreases stromal cell migration and embryo adhesion. Our findings highlight the crucial role of Lox in endometrial stromal cells and deepen our understanding of decidualization.